INVITRO TRIMERIZATION OF OMPF PORIN SECRETED BY SPHEROPLASTS OF ESCHERICHIA-COLI

被引：77

作者：

SEN, K

NIKAIDO, H

机构：

[1] Department of Molecular Biology, University of California, Berkeley

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 02期

关键词：

Lipopolysaccharide; Outer membrane; Protein secretion; Protein targeting;

D O I：

10.1073/pnas.87.2.743

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

It is not yet clear how bacterial outer membrane proteins reach their correct destination after they are secreted across the cytoplasmic membrane. We show here that porin OmpF is secreted into the medium as a water-soluble monomeric protein by spheroplasts of Escherichia coli. Furthermore, this monomeric porin is taken up by cell envelope preparations or purified lipopolysaccharides in the presence of 0.03% Triton X-100 and is converted correctly into the mature trimeric conformation. These results appear to reproduce a part of the physiological export and targeting steps of this protein.

引用

页码：743 / 747

页数：5

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